ID   PYRG_BORAP              Reviewed;         533 AA.
AC   Q0SMT3;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   16-JUN-2009, entry version 24.
DE   RecName: Full=CTP synthase;
DE            EC=6.3.4.2;
DE   AltName: Full=UTP--ammonia ligase;
DE   AltName: Full=CTP synthetase;
GN   Name=pyrG; OrderedLocusNames=BAPKO_0606;
OS   Borrelia afzelii (strain PKo).
OC   Bacteria; Spirochaetes; Spirochaetales; Spirochaetaceae; Borrelia;
OC   Borrelia burgdorferi group.
OX   NCBI_TaxID=390236;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16914037; DOI=10.1186/1471-2164-7-211;
RA   Gloeckner G., Schulte-Spechtel U., Schilhabel M., Felder M.,
RA   Suehnel J., Wilske B., Platzer M.;
RT   "Comparative genome analysis: selection pressure on the Borrelia vls
RT   cassettes is essential for infectivity.";
RL   BMC Genomics 7:211-211(2006).
CC   -!- FUNCTION: Catalyzes the ATP-dependent amination of UTP to CTP with
CC       either L-glutamine or ammonia as the source of nitrogen (By
CC       similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + UTP + NH(3) = ADP + phosphate + CTP.
CC   -!- ENZYME REGULATION: Allosterically activated by GTP, when glutamine
CC       is the substrate. Inhibited by CTP (By similarity).
CC   -!- PATHWAY: Pyrimidine metabolism; CTP biosynthesis via de novo
CC       pathway; CTP from UDP: step 2/2.
CC   -!- SUBUNIT: Homotetramer (By similarity).
CC   -!- SIMILARITY: Belongs to the CTP synthase family.
CC   -!- SIMILARITY: Contains 1 glutamine amidotransferase type-1 domain.
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DR   EMBL; CP000395; ABH01845.1; -; Genomic_DNA.
DR   RefSeq; YP_710021.1; -.
DR   GeneID; 4227309; -.
DR   GenomeReviews; CP000395_GR; BAPKO_0606.
DR   KEGG; baf:BAPKO_0606; -.
DR   NMPDR; fig|390236.5.peg.631; -.
DR   HOGENOM; Q0SMT3; -.
DR   OMA; Q0SMT3; EFNNAYR.
DR   BioCyc; BAFZ390236:BAPKO_0606-MON; -.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003883; F:CTP synthase activity; IEA:HAMAP.
DR   GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0006221; P:pyrimidine nucleotide biosynthetic process; IEA:HAMAP.
DR   HAMAP; MF_01227; -; 1.
DR   InterPro; IPR004468; CTP_synthase.
DR   InterPro; IPR017456; CTP_synthase_N.
DR   InterPro; IPR017926; GATASE_1.
DR   InterPro; IPR000991; GATase_class1_C.
DR   PANTHER; PTHR11550; PyrG_synth; 1.
DR   Pfam; PF06418; CTP_synth_N; 1.
DR   Pfam; PF00117; GATase; 1.
DR   TIGRFAMs; TIGR00337; PyrG; 1.
DR   PROSITE; PS51273; GATASE_TYPE_1; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Complete proteome; Glutamine amidotransferase; Ligase;
KW   Nucleotide-binding; Pyrimidine biosynthesis.
FT   CHAIN         1    533       CTP synthase.
FT                                /FTId=PRO_0000266076.
FT   DOMAIN      304    533       Glutamine amidotransferase type-1.
FT   REGION        1    256       Aminator domain.
FT   ACT_SITE    382    382       Nucleophile (By similarity).
FT   ACT_SITE    511    511       By similarity.
FT   ACT_SITE    513    513       By similarity.
SQ   SEQUENCE   533 AA;  59586 MW;  84E463023F3269A1 CRC64;
     MKKNLKILVI TGGVISGIGK GVTSASIARL FRYDFRVTPI KCDGYLNTDP GTINPVEHGE
     VFVLDDGGEV DMDFGHYERF LNLNAKSSWN ITMGKIYKKI LENERKGKYL GRTVQLIPHV
     TDEIKSTIFQ IASSENSEML IIEIGGTVGD MENILFIETV RQIRHEVGSG NIAFIHLTYV
     PSPVGINEQK SKPTQQSVKT LNKAGIFPDL IIARSSQVLT DQIRKKIAMF CNVESTSIID
     NIDVSTIYEI PISFYKQGVH EILSSKLNIK VDPKIEELSR LVGIIKSNFF VPKKIINIAI
     CGKYAELDDS YASIRESLVH VAANLDLLIK STLIDSNDLN ESCLKDFDGI IVPGGFGGKG
     YEGKIIAIKY ARENNIPFLG ICLGLQLAVI EFARNVCGIL DADTEENLIK DKPLKNPVIH
     LLPEQKEIKD KGATMRLGGY PVILKKNTIA FKLYGQDRII ERFRHRYEVN NDYIDLFEKN
     GLIVSGFSSD FKIAKLIEIP KNKFFVACQF HPELITRIEN PAKLFLGLIK ACI
//